Title
Establishment of the enzymatic protein acetylation independent of acetyl CoA: Recombinant glutathione S-transferase 3-3 is acetylated by a novel membrane-bound transacetylane using 7,8-diacetoxy-4-methyl coumarin as the acetyl donor
Author
Kohli, E.
Gaspari, M.
Raj, H.G.
Parmar, V.S.
van der Greef, J.
Gupta, G.
Kumari, R.
Prasad, A.K.
Goel, S.
Pal, G.
Tyagi, K.
Jain, S.C.
Ahmad, N.
Watterson, A.C.
Olsen, C.E.
Centraal Instituut voor Voedingsonderzoek TNO TNO Voeding
Publication year
2002
Abstract
The current knowledge on biological protein acetylation is confined to acetyl CoA-dependent acetylation of protein catalyzed by specific acetyl transferases and the non-enzymatic acetylation of protein by acetylated xenobiotics such as aspirin. We have discovered a membrane-bound enzyme catalyzing the transfer of acetyl groups from the acetyl donor 7,8-diacetoxy-4-methyl coumarin (DAMC) to glutathione S-transferase 3-3 (GST3-3), termed DAMC:protein transacetylase (TAase). The purified enzyme was incubated with recombinant GST3-3 subunit and DAMC, the modified protein was isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in gel digested with trypsin and the tryptic digest was analyzed by mass spectrometry. The N-terminus and six lysines, Lys-51, -82, -124, -181, -191 and -210, were found to be acetylated. The acetylation of GST3-3 described above was not observed in the absence of either DAMC or TAase. These results clearly establish the phenomenon of protein acetylation independent of acetyl CoA catalyzed by a hitherto unknown enzyme (TAase) utilizing a certain xenobiotic acetate (DAMC) as the active acetyl donor. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. Chemicals/CAS: 7,8-diacetoxy-4-methylcoumarin; Acetyl Coenzyme A, 72-89-9; Acetylesterase, EC 3.1.1.6; Coumarins; Glutathione Transferase, EC 2.5.1.18; Recombinant Proteins
Subject
Acetyl Coenzyme A
Acetylation
Acetylesterase
Coumarins
Glutathione Transferase
Recombinant Proteins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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http://resolver.tudelft.nl/uuid:cbf9b458-5954-4a6f-b4ae-a37d900a4c6b
DOI
https://doi.org/10.1016/s0014-5793(02)03445-2
TNO identifier
87760
Source
FEBS Letters, 530 (1-3), 139-142
Document type
article